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Interactions of troponin subunits with different forms of tropomyosin

Authors
Journal
Journal of Ultrastructure Research
0022-5320
Publisher
Elsevier
Publication Date
Volume
48
Issue
1
Identifiers
DOI: 10.1016/s0022-5320(74)80043-2
Disciplines
  • Mathematics

Abstract

Tropomyosin from rabbit skeletal muscle has been separated into fractions containing only 34 000 dalton chains (SB-TM) and fractions containing both 34 000 and 36 000 dalton chains (DB-TM). Both SB-TM and DB-TM formed crystals and tactoids with a common 400 Å repeat. In addition the SB-TM gave a new crystal type which has not been described in studies on unfractionated tropomyosin. TN-T interacted with both tropomyosin forms to give a variety of geometric patterns, some of which have been previously ascribed to tropomyosin alone. TN-I inhibited tropomyosin tactoid formation, suggesting some type of direct interaction. TN-C, however, had no effect on the formation of tropomyosin crystals or tactoids or on their appearance.

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